Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for P9WHM2

Entry ID Method Resolution Chain Position Source
AF-P9WHM2-F1 Predicted AlphaFoldDB

No variants for P9WHM2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P9WHM2

No associated diseases with P9WHM2

4 regional properties for P9WHM2

Type Name Position InterPro Accession
domain Formyl transferase, N-terminal 116 - 292 IPR002376
domain ACT domain 32 - 108 IPR002912
domain Formyltetrahydrofolate deformylase, C-terminal hydrolase domain 116 - 310 IPR041729
domain Formyltetrahydrofolate deformylase, ACT domain 32 - 107 IPR044074

Functions

Description
EC Number 3.5.1.10 In linear amides
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

1 GO annotations of molecular function

Name Definition
formyltetrahydrofolate deformylase activity Catalysis of the reaction: 10-formyltetrahydrofolate + H(2)O = (6S)-5,6,7,8-tetrahydrofolate + formate + H(+).

2 GO annotations of biological process

Name Definition
'de novo' IMP biosynthetic process The chemical reactions and pathways resulting in the formation of IMP, inosine monophosphate, by the stepwise assembly of a purine ring on ribose 5-phosphate.
one-carbon metabolic process The chemical reactions and pathways involving the transfer of one-carbon units in various oxidation states.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MGKGSMTAHA TPNEPDYPPP PGGPPPPADI GRLLLRCHDR PGIIAAVSTF LARAGANIIS
70 80 90 100 110 120
LDQHSTAPEG GTFLQRAIFH LPGLTAAVDE LQRDFGSTVA DKFGIDYRFA EAAKPKRVAI
130 140 150 160 170 180
MASTEDHCLL DLLWRNRRGE LEMSVVMVIA NHPDLAAHVR PFGVPFIHIP ATRDTRTEAE
190 200 210 220 230 240
QRQLQLLSGN VDLVVLARYM QILSPGFLEA IGCPLINIHH SFLPAFTGAA PYQRARERGV
250 260 270 280 290 300
KLIGATAHYV TEVLDEGPII EQDVVRVDHT HTVDDLVRVG ADVERAVLSR AVLWHCQDRV
IVHHNQTIVF